Biochemical characterization of the lizard toxin gilatoxin.
The Gila monster (genus Heloderma) is the only known lizard to produce and inject a venomous secretion. Little is known about the venom from these lizards, and none of the toxins have been isolated until this time. This paper reports the isolation and characterization of a major lethal toxin (gilatoxin) from the venoms of Heloderma suspectum and Heloderma horridum. Gilatoxins from both species were similar in amino acid composition, electrophoretic mobility, pI, and immunological reactivity. They are acidic proteins possessing molecular weights of 35 000-37 500 and isoelectric points of 4.25 and consist of a single polypeptide chain. Neither is antigenically related to the venoms of snakes. The toxins are devoid of phospholipase A2 activity and proteolytic, hemorrhagic, and hemolytic activities, with lethality being the only biological activity detectably expressed. The toxins appear to be unique and distinct from those of other venomous animals.
D000478:Alkylation; D000596:Amino Acids / Q000032:analysis; D000664:Amphibian Venoms / Q000302:isolation & purification*; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D006023:Glycoproteins / Q000032:analysis; D005779:Immunodiffusion; D008116:Lizards; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010455:Peptides; D013045:Species Specificity
D000596:Amino Acids; D000664:Amphibian Venoms; D000906:Antibodies; D000936:Antigen-Antibody Complex; D006023:Glycoproteins; D010455:Peptides; C031673:gilatoxin